ArticleScientific reports2017
Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 16 citations in OpenAlex.
- Mapping the effects of specific radiation damage and solvent radiolysis in buffers and crystals with online UV-Vis absorption spectroscopy.Acta crystallographica. Section D, Structural biology · 2026Article
- Structure of mycobacterial ergothioneine-biosynthesis C-S lyase EgtE.The Journal of biological chemistry · 2024Article
- Inhibition of 3-Hydroxykynurenine Transaminase fromACS bio & med chem Au · 2023Article
- Identification of Human Alanine-Glyoxylate Aminotransferase Ligands as Pharmacological Chaperones for Variants Associated with Primary Hyperoxaluria Type 1.Journal of medicinal chemistry · 2022Article
- Structural dynamics shape the fitness window of alanine:glyoxylate aminotransferase.Protein science : a publication of the Protein Society · 2022Article
- Development and characterization of a glycine biosensor system for fine-tuned metabolic regulation in Escherichia coli.Microbial cell factories · 2022Article
- Crystal structure of Aspergillus fumigatus AroH, an aromatic amino acid aminotransferase.Proteins · 2022Article
- Crystal Structure Of Photorespiratory Alanine:Glyoxylate Aminotransferase 1 (AGT1) FromFrontiers in plant science · 2019Article
- Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis.The Journal of biological chemistryArticle
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6 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The alanine:glyoxylate aminotransferase (AGT), a hepatocyte-specific pyridoxal-5'-phosphate (PLP) dependent enzyme, transaminates L-alanine and glyoxylate to glycine and pyruvate, thus detoxifying glyoxylate and preventing pathological oxalate precipitation in tissues. In the widely accepted catalytic mechanism of the aminotransferase family, the lysine binding to PLP acts as a catalyst in the stepwise 1,3-proton transfer, interconverting the external aldimine to ketimine. This step requires protonation by a conserved aspartate of the pyridine nitrogen of PLP to enhance its ability to stabilize the carbanionic intermediate. The aspartate residue is also responsible for a significant geometrical distortion of the internal aldimine, crucial for catalysis. We present the structure of human AGT in which complete X-ray photoreduction of the Schiff base has occurred. This result, together with two crystal structures of the conserved aspartate pathogenic variant (D183N) and the molecular modeling of the transaldimination step, led us to propose that an interplay of opposite forces, which we named spring mechanism, finely tunes PLP geometry during catalysis and is essential to move the external aldimine in the correct position in order for the 1,3-proton transfer to occur.
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